ExplorEnz: EC 3.4.22.50

Your query returned 1 entry. Printable version

3.4.22.50

Accepted name:

V-cath endopeptidase

Reaction:

Endopeptidase of broad specificity, hydrolysing substrates of both cathepsin L and cathepsin B

Other name(s):

AcNPV protease; BmNPV protease; NPV protease; baculovirus cathepsin; nucleopolyhedrosis virus protease; viral cathepsin

Comments:

In peptidase family C1. Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, CAS registry number: 316365-69-2

References:

1.	Slack, J.M., Kuzio, J. and Faulkner, P. Characterization of V-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis-virus. J. Gen. Virol. 76 (1995) 1091–1098. [DOI] [PMID: 7730794]
2.	Hawtin, R.E., Zarkowska, T., Arnold, K., Thomas, C.J., Gooday, G.W., King, L.A., Kuzio, J.A. and Possee, R.D. Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes. Virology 238 (1997) 243–253. [DOI] [PMID: 9400597]

[EC 3.4.22.50 created 2003]